Anti-PKA beta (catalytic subunit) (phospho S338) antibody (ab5816)
Key features and details
- Rabbit polyclonal to PKA beta (catalytic subunit) (phospho S338)
- Suitable for: WB
- Reacts with: Mouse
- Isotype: IgG
Overview
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Product name
Anti-PKA beta (catalytic subunit) (phospho S338) antibody
See all PKA beta (catalytic subunit) primary antibodies -
Description
Rabbit polyclonal to PKA beta (catalytic subunit) (phospho S338) -
Host species
Rabbit -
Specificity
Peptide competition data indicate that this antibody cross-reacts with the PKA nu subunit (64% homologous) and partially with the alpha subunit (82% homologous). -
Tested Applications & Species
See all applications and species dataApplication Species WB Mouse
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Immunogen
Synthetic phosphopeptide derived from a region of human PKA catalytic beta subunit that contains serine 338.
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Positive control
- 3T3-L1 adipocytes.
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General notes
c-AMP-dependent Protein Kinase (PKA) is a serine/threonine kinase that regulates a number of cellular processes including proliferation, ion transport and gene transcription. PKA is composed of conserved catalytic subunits and regulatory subunits that dissociate upon activation by cAMP. The catalytic subunit of PKA contains the activation loop and mediates DNA binding and substrate recognition. The catalytic subunit is assembled and expressed as an active form and is phosphorylated on threonine 197 by PDK 1 in the activation loop and serine 338 in the carboxyl terminus. Phosphorylation of serine 338 plays a key role in stabilizing PKA and activating its substrates, and hence mediating its biological functions.
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. -
Storage buffer
pH: 7.30
Preservative: 0.05% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA -
Concentration information loading... -
Purity
Immunogen affinity purified -
Purification notes
The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated PKA. The final product is generated by affinity chromatography using a PKA-derived peptide that is phosphorylated at serine 338. -
Primary antibody notes
c-AMP-dependent Protein Kinase (PKA) is a serine/threonine kinase that regulates a number of cellular processes including proliferation, ion transport and gene transcription. PKA is composed of conserved catalytic subunits and regulatory subunits that dissociate upon activation by cAMP. The catalytic subunit of PKA contains the activation loop and mediates DNA binding and substrate recognition. The catalytic subunit is assembled and expressed as an active form and is phosphorylated on threonine 197 by PDK 1 in the activation loop and serine 338 in the carboxyl terminus. Phosphorylation of serine 338 plays a key role in stabilizing PKA and activating its substrates, and hence mediating its biological functions. -
Clonality
Polyclonal -
Isotype
IgG -
Research areas
Images
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Western blot - Anti-PKA beta (catalytic subunit) (phospho S338) antibody (ab5816)Peptide Competition: Lysates prepared from 3T3-L1 cells were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were either treated with lambda phosphatase (1) or left untreated (2-5), blocked with a 5% BSA-TBSTbuffer for two hours at room temperature, and incubated with ab5816 antibody for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1, 2), the non-phosphopeptide corresponding to the immunogen (3), a generic phosphoserine-containing peptide (4), or, the phosphopeptide immunogen (5). After washing, membranes were incubated with goat F(ab’)2 anti-rabbit IgG HRP-conjugate and bands were detected using the Pierce SuperSignalTM method. The data show that the peptide corresponding to PKA cat beta [pS338] blocks the antibody signal, thereby verifying the specificity of the antibody. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
Peptide Competition: Lysates prepared from 3T3-L1 cells were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were either treated with lambda phosphatase (1) or left untreated (2-5), blocked with a 5% BSA-TBSTbuffer for two hours at room temperature, and incubated with ab5816 antibody for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1, 2), the non-phosphopeptide corresponding to the immunogen (3), a generic phosphoserine-containing peptide (4), or, the phosphopeptide immunogen (5). After washing, membranes were incubated with goat F(ab’)2 anti-rabbit IgG HRP-conjugate and bands were detected using the Pierce SuperSignalTM method. The data show that the peptide corresponding to PKA cat beta [pS338] blocks the antibody signal, thereby verifying the specificity of the antibody. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
